Linked Life Data

8390373

Source:http://linkedlifedata.com/resource/pubmed/id/8390373

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1993-7-22
pubmed:abstractText
The merits of the suggestion that CuA in cytochrome oxidase is a mixed-valence binuclear site is reviewed on the basis of recent analytical and spectroscopic studies. First an alternative mononuclear model is presented. Metal analyses indicate that homogeneous oxidase preparations with high activity contain 3Cu/2Fe. Multifrequency EPR measurements demonstrate a close similarity with a copper site in nitrous oxide reductase, and this is also supported by optical and MCD spectra. Strong evidence for a binuclear site is provided by a 7-line hyperfine structure in the EPR spectra of both enzymes. A binuclear model consistent with amino acid sequence data can be formulated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
325
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49-52
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The nature of the CuA center in cytochrome c oxidase.
pubmed:affiliation
Department of Biochemistry and Biophysics, University of Göteborg, Sweden.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't